ID   GATA_IXOSC              Reviewed;         505 AA.
AC   B7PDC5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03150};
DE            Short=Glu-AdT subunit A {ECO:0000255|HAMAP-Rule:MF_03150};
DE            EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_03150};
GN   Name=gatA {ECO:0000255|HAMAP-Rule:MF_03150}; ORFNames=ISCW003184;
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel;
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in the
CC       mitochondria. The reaction takes place in the presence of glutamine and
CC       ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC       {ECO:0000255|HAMAP-Rule:MF_03150}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03150};
CC   -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC       complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_03150}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR   EMBL; DS689337; EEC04597.1; -; Genomic_DNA.
DR   RefSeq; XP_002410727.1; XM_002410682.1.
DR   AlphaFoldDB; B7PDC5; -.
DR   SMR; B7PDC5; -.
DR   STRING; 6945.B7PDC5; -.
DR   GeneID; 8028239; -.
DR   KEGG; isc:IscW_ISCW003184; -.
DR   VEuPathDB; VectorBase:ISCI003184; -.
DR   VEuPathDB; VectorBase:ISCW003184; -.
DR   HOGENOM; CLU_009600_7_6_1; -.
DR   InParanoid; B7PDC5; -.
DR   OMA; EVSCPHF; -.
DR   OrthoDB; 1195292at2759; -.
DR   PhylomeDB; B7PDC5; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR004412; GatA.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..505
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT                   mitochondrial"
FT                   /id="PRO_0000413338"
FT   ACT_SITE        76
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        158
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT   ACT_SITE        182
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
SQ   SEQUENCE   505 AA;  54007 MW;  5E6005FC73683F7D CRC64;
     MLSLTIKELV SHFKAKKCSP VDICATCIKE INDSSFLNAF VTVLPEAAEK QARESHARWK
     SGKPRGPLDG VPIAVKDNFC MTGVRTTCGS RMLANFYPPY TATVVERLQG EGAVVLGKTN
     MDEFGMGSGA TDSAFGPTKN PWKNAGEAAD DWYITGGSSG GSAVAVATGC SFGALGSDTG
     GSTRNPASRC GVVGLKPTYG ALSRHGLIPL TNSMDVPGIL AKCVDDAAVL LSATACADPN
     DSTSVSAPDS VRHLKLAGEP SLKGVKIGVP KEYHCPGMCP EVLDLWRDVA DRLAALGAVV
     SSVSLPHSRY STECYSVLNC CEVASNFARY DGLEYGHRAS DDSSTDALYA ASRHEGLNEV
     VRGRILAGNY FLLRANYEKY FTKALQVRRL ISDDFTKVFA SGVELLLTPV TLTAALRHSE
     WTLKDNRERA SVEDFCTQPV NMAGLPAVSV PCRLSREGLP LSLQLVGPKF SEAAMLAAAK
     RLELELSFPR LDLQLHAHQE SYATL